The three-dimensional structure of the seed storage protein phaseolin at 3 A resolution.
The polypeptides of the trimeric seed storage protein phaseolin comprise two structurally similar units each made up of a beta-barrel and an alpha-helical domain. The beta-barrel has the 'jelly-roll' folding topology of the viral coat proteins and the alpha-helical domain shows structural similarity to the helix-turn-helix motif found in certain DNA-binding proteins.
Lawrence
M C
MC
CSIRO Division of Biotechnology, Parkville, Victoria, Australia.
Suzuki
E
E
Varghese
J N
JN
Davis
P C
PC
Van Donkelaar
A
A
Tulloch
P A
PA
Colman
P M
PM
D000595:Amino Acid Sequence; D001665:Binding Sites; D003460:Crystallization; D006031:Glycosylation; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010940:Plant Proteins; D011487:Protein Conformation; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D010940:Plant Proteins; C048826:phaseolin protein, Phaseolus vulgaris